Short communicationIsolation and pharmacological characterization of a new α-neurotoxin (α-AgTx) from venom of the viper Ackistrodon halys (Pallas)
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Cited by (12)
Synergistic strategies of predominant toxins in snake venoms
2018, Toxicology LettersCitation Excerpt :3FTxs are non-enzymatic polypeptides containing 60–74 amino acid residues (Dufton and Hider, 1988). They are found abundantly in the venoms of elapids (cobras, kraits and mambas) (Fry et al., 2003a) and hydrophis (sea snakes) (Pahari et al., 2007a), and have recently been found in the venoms of colubrids (Fry et al., 2003b; Pawlak et al., 2006; Lumsden et al., 2005; Pawlak et al., 2009) and the venom gland transcriptomes of viperids and crotalids (Jiang et al., 1987; Junqueira-de-Azevedo et al., 2006; Pahari et al., 2007b). Structurally, 3FTxs have three distinct β-stranded loops extending from a small, globular, hydrophobic core that is cross-linked by four conserved disulfide bridges.
Proteomic characterization and comparison of venoms from two elapid snakes (Bungarus multicinctus and Naja atra) from China
2016, Journal of ProteomicsCitation Excerpt :To test this idea, we should enhance the immune response of these components when designing or re-designing commercial antivenoms to neutralize B. multicinctus and N. atra venoms. Generally, 3-FTxs are commonly found and recognized as a large group of non-enzymatic toxins in the venoms of elapid, hydrophiid and colubrid snakes [1,54–56] and in the venom gland transcriptomes of some crotalid snakes [57–59]. In practice, long chain α-neurotoxin (Type II α-neurotoxin), κ-neurotoxin and orphan group V (formerly γ-neurotoxin) of 3-FTxs are thought to act as postsynaptic neurotoxins, and are respectively demonstrated to be peripheral and neuronal nicotinic acetylcholine receptor (AChRs) antagonists [49,60–62] that cause paralysis, respiratory failure and death.
Structure, function and evolution of three-finger toxins: Mini proteins with multiple targets
2010, ToxiconCitation Excerpt :This family of non-enzymatic polypeptides contains 60–74 amino acid residues (Dufton and Hider, 1988; Endo and Tamiya, 1991). They are found in the venoms of elapids (cobras, kraits and mambas), hydrophiids (sea snakes), and colubrids (Pawlak et al., 2006, 2009) as well as reported in the transcriptomes of viperids and crotalids (Jiang et al., 1987; Pahari et al., 2007). Similar to other snake venom proteins, 3FTxs are also rich in disulphide bonds.
Structural and functional characterization of a novel homodimeric three-finger neurotoxin from the venom of Ophiophagus hannah (King cobra)
2010, Journal of Biological ChemistryCitation Excerpt :They are most commonly found in the venoms of elapid and hydrophiid snakes. Recently, our laboratory has also demonstrated the presence of 3FTxs from colubrid venoms (12, 13), and 3FTx transcripts have been found in the venom gland transcriptome of viperid snakes (14, 15). The proteins in this family of toxins share a common structural scaffold of three β-sheeted loops emerging from a central core (11, 16).
What Are the Neurotoxins in Hemotoxic Snake Venoms?
2023, International Journal of Molecular Sciences